ID BGAL_OENOB Reviewed; 1031 AA.
AC Q04F24;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 29-MAY-2013, entry version 49.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=lacZ; OrderedLocusNames=OEOE_1044;
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Oenococcus.
OX NCBI_TaxID=203123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC galactose residues in beta-D-galactosides.
CC -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000411; ABJ56948.1; -; Genomic_DNA.
DR RefSeq; YP_810613.1; NC_008528.1.
DR ProteinModelPortal; Q04F24; -.
DR STRING; 203123.OEOE_1044; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; ABJ56948; ABJ56948; OEOE_1044.
DR GeneID; 4415716; -.
DR KEGG; ooe:OEOE_1044; -.
DR PATRIC; 22800265; VBIOenOen113004_1059.
DR eggNOG; COG3250; -.
DR HOGENOM; HOG000252443; -.
DR KO; K01190; -.
DR OMA; FFRAPLD; -.
DR ProtClustDB; PRK09525; -.
DR BioCyc; OOEN203123:GHNL-1044-MONOMER; -.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; -; 1.
DR Gene3D; 2.60.40.320; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 3.20.20.80; -; 1.
DR HAMAP; MF_01687; Beta_gal; 1; -.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR006103; Glyco_hydro_2_TIM.
DR InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF74650; Gal_mut_like; 1.
DR SUPFAM; SSF49303; Glyco_hydro_2Ig; 2.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW Sodium.
FT CHAIN 1 1031 Beta-galactosidase.
FT /FTId=PRO_0000367004.
FT REGION 533 536 Substrate binding (By similarity).
FT ACT_SITE 457 457 Proton donor (By similarity).
FT ACT_SITE 533 533 Nucleophile (By similarity).
FT METAL 197 197 Sodium (By similarity).
FT METAL 412 412 Magnesium 1 (By similarity).
FT METAL 414 414 Magnesium 1 (By similarity).
FT METAL 457 457 Magnesium 1 (By similarity).
FT METAL 593 593 Magnesium 2 (By similarity).
FT METAL 597 597 Sodium; via carbonyl oxygen (By
FT similarity).
FT METAL 600 600 Sodium (By similarity).
FT BINDING 98 98 Substrate (By similarity).
FT BINDING 197 197 Substrate (By similarity).
FT BINDING 457 457 Substrate (By similarity).
FT BINDING 600 600 Substrate (By similarity).
FT BINDING 1005 1005 Substrate (By similarity).
FT SITE 353 353 Transition state stabilizer (By
FT similarity).
FT SITE 387 387 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 1031 AA; 118758 MW; ABBC52BF9A20F31B CRC64;
MTNKISFRDI INRKDWENPV ITNWHRLPIH TEMNYSKSLN EDKQKTIQSL NGNWCFSYFS
KVTDVPENWA DRDLTKSNIM PVPSNWQLHG YDQPIYSNVA YPFPANPPYL PEENPTACYS
RIFQLNDDWL QSGQNHVIFN GVGSAFHLWL NGQWIGYSED SRLPAEFDLT KYLKSGKNRI
SVMVLRWSKG SYFEDQDMWR MSGIFRDVEV KHLPATYLQD YQLQTDLDDD LDQAKITIKA
QVAGKNFSQN KLRTRLYFAN EKVADQSSRL STRAVDERGP LDNQFIAELN LKDPYLWSAE
LPYLYQLVIE LLTDDGDILQ VEKVNIGVRK VEIKNGLLKL NGKPLLIRGT NKHEFDSKKG
YAVDEETMIQ DIKAMKRNNF NAVRCSHYPN NRRWYELCDQ YGLYVVDEAN IETHGMVPMN
RLTNDPVYLP LMSDRVTRMV TRDRNHPSII IWSLGNESGY GRNHAALYNW IKQSDLSRPV
QYEGGGANTA VTDIIVPMYA RVEQDQIESV NSKWSLKKWI GLPGETRPLI LCEYAHDMGN
SLGGFGKYWQ AFHKYPRLQG GFIWDWVDQG LLKKDVNGND FYAYGGDFKD QPNDRQFCLD
GLLFPDRTPK PAMHEVKYWQ QYYLFNLQRN PLGQAESFTV TNDYSFKKSS NERLHYQIKS
ENEIVIDKYI DLVLNPGESL LIKLPKGRSS TSSLLDIDIS LIKGNSWAPS GFKIASEQYV
LAKKFGPTNA VTAATNKISL IENKDTNTFE IKLDDQKWQF AKNSGLLVSW SKSGNENLLD
ALRDQFTRAP LDNDIGVSKV DHIDPNAWYE RWKSAGMYNL KTNLVSIDAE QLERAVLIRT
EHSYSNHFQI LFKSSKIYRI DANGTMTVTV DVSLAQGIPF PARIGLTCHL ADQITDVSYT
GLGPFENYPD RQSAAQYGHW QMELDDLYTP YIFPSENGSR GQVSQLEFGK QKISAYHEQN
FSFNLSRFSK QQLARISHRN LLQAENGVWL SIDGYRMGVG GDDSWSPSVA PEYLLSNNYY
HYAFQWCRKD I
//
